Calmin, a Protein with Calponin Homology and Transmembrane Domains Expressed in Maturing Spermatogenic Cells

A cDNA named calmin of ∼3.2 kb was isolated by RNA differential display applied to developing mouse skin. Calmin cDNA encodes 1021 amino acids with two calponin homology (CH) domains in tandem on the N-terminal side and a transmembrane domain on the C-terminal side. The region covering the CH domain...

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Bibliographic Details
Published in:Genomics (San Diego, Calif.) Calif.), 2001-06, Vol.74 (2), p.172-179
Main Authors: Ishisaki, Zenji, Takaishi, Mikiro, Furuta, Isao, Huh, Nam-ho
Format: Article
Language:English
Subjects:
Actinin - chemistry
Alternative Splicing
Amino Acid Sequence
Animals
Base Sequence
Biological and medical sciences
Blotting, Northern
Blotting, Western
Calcium-Binding Proteins - chemistry
Calmin
Calponin
Calponins
Cell Membrane - metabolism
COS Cells
DNA, Complementary - metabolism
Dystrophin - chemistry
Exons
Fundamental and applied biological sciences. Psychology
Genes. Genome
Humans
In Situ Hybridization
Introns
Male
Membrane Proteins - chemistry
Membrane Proteins - genetics
Mice
Microfilament Proteins
Models, Genetic
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
Protein Structure, Tertiary
Reverse Transcriptase Polymerase Chain Reaction
Skin - embryology
spectrin
Spectrin - chemistry
Spermatocytes - metabolism
Testis - metabolism
Time Factors
Tissue Distribution
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Summary:A cDNA named calmin of ∼3.2 kb was isolated by RNA differential display applied to developing mouse skin. Calmin cDNA encodes 1021 amino acids with two calponin homology (CH) domains in tandem on the N-terminal side and a transmembrane domain on the C-terminal side. The region covering the CH domains showed a high level of homology with β-spectrin, α-actinin, and dystrophin. Among the proteins with the tandem CH domains, calmin is unique in having a transmembrane domain. Three alternative splicing sites were identified at the 3′-side of calmin, giving rise to polymorphic protein products with or without the transmembrane domain. The calmin transcript was detected in adult testis, liver, kidney, and large intestine; the expression in testis was far stronger than that in the other tissues. In situ hybridization and immunostaining revealed that calmin was expressed in maturing spermatogenic cells at later stages. Human calmin cDNA was also isolated, and its exon/intron organization was determined.
ISSN:0888-7543
1089-8646
DOI:10.1006/geno.2001.6544